Enzymatic characteristics of polyphenoloxidase from shrimp (Penaeus vannamei) and its inhibition by a novel hydroxypyridinone derivative.

Abstract

Melanosis developed in shrimp (Penaeus vannamei) is mainly initiated by polyphenoloxidase (PPO), thus understanding of the characteristics of PPO in shrimp is important for controlling the melanosis of shrimp. The shrimp cephalothorax turns black most rapidly amongst all the tissues during the chilled storage. Crude PPO extracted from this cephalothorax has an optimal pH of 6.0 and an optimal temperature of 50°C. PPO is relatively stable under neutral and weak alkaline conditions (pH 5.5-9.0) and the temperature range of 25-35°C. The kinetic parameters K m and V max were recorded as 3.02mM and 54.3U/mg of protein, respectively, using L-Dopa as a substrate. The molecular weight of PPO was estimated as 200-220kDa by an activity staining test. A hydroxypyridinone derivative, 5-hydroxy-1-octyl-4-oxo-1,4-dihydropyridine-2-carbaldehyde O-ethyl oxime, was demonstrated to efficiently inhibit the PPO, indicating that this compound might find application as a shrimp preservative.